ThiC Is an [Fe-S] Cluster Protein That Requires AdoMet To Generate the 4-Amino-5-hydroxymethyl-2-methylpyrimidine Moiety in Thiamin Synthesis†

N. Cecilia Martinez-Gomez and Diana M. Downs*
Department of Bacteriology, University of Wisconsin, 1550 Linden Drive, Madison, Wisconsin 53706
Biochemistry, 2008, 47 (35), pp 9054–9056
DOI: 10.1021/bi8010253
Publication Date (Web): August 8, 2008
Copyright © 2008 American Chemical Society
†

This work was supported by Competitive Grant GM47296 from the NIH and funds from a 21st Century Scientists Scholars Award from the J. M. McDonnell fund.

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* To whom correspondence should be addressed. E-mail: downs@bact.wisc.edu. Telephone: (608) 265-4630. Fax: (608) 262-9865.

Abstract

Abstract Image

Thiamin pyrophosphate is a required cofactor in all organisms. The biosynthesis of thiamin requires the independently synthesized 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate (HMP-PP) and 5-hydroxyethyl-4-methylthiazole phosphate (THZ-P) moieties. In bacteria, the pyrimidine moiety is derived from 5-aminoimidazole ribotide (AIR), and ThiC is the only gene product known to be required for this conversion in vivo. We report here the purification and characterization of the ThiC protein from Salmonella enterica. The data showed this protein generated HMP when AIR, S-adenosylmethionine (AdoMet), and an appropriate reducing agent were present. It is further shown that ThiC carries an oxygen labile [Fe-S] cluster essential for this activity.

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History

  • Published In Issue September 02, 2008
  • Article ASAPAugust 08, 2008
  • Received: June 6, 2008
    Revised: July 23, 2008

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